654results about "Polypeptide with His-tag" patented technology

The present invention relates to modified Dda helicases which can be used to control the movement of analytes such as polynucleotides. The modified Dda helicases are used in analyte detection and characterisation. The present invention also relates to novel protein pores and their uses in analyte detection and characterisation. The invention particularly relates to an isolated pore complex formed by a CsgG-like pore and a modified CsgF peptide, or a homologue or mutant thereof, thereby incorporating an additional channel constriction or reader head in the nanopore.

Disclosed herein are monospecific and multi-specific antibodies with specificities for one or more of OX40, CD40, 4-1BB, HSA, IL-22, or EGFR. Specifically, the disclosure provides variable heavy (VHH) domains of the antibodies with specificities for one or more of OX40, CD40, 4-1BB, HSA, IL-22, or EGFR, and associated sequences. Further discloses are methods of using the monospecific or multi-specific antibodies for treating ah autoimmune disease.

The invention discloses a method for improving the solubility and thermal stability of sweet protein, and belongs to the technical field of biosynthesis, the method comprises the following steps: constructing a gene tandem recombinant plasmid containing a monellin x-3C-sfGFP-3C-monellin y expression cassette, x is greater than or equal to 1, y is greater than or equal to 1, 5 is greater than or equal to x + y is greater than or equal to 3, a 3C protease recognition sequence is also inserted between adjacent copies of monellin, and each monellin is connected with a purification tag; the gene tandem recombinant plasmid is transformed into escherichia coli and inducible expression is carried out, thalli are split and purified to obtain fusion protein, 3C protease is used for enzyme digestion, and the target protein is obtained after re-purification. The total protein yield and the solubility proportion are remarkably improved by adopting a series construction mode of plasmids, meanwhile, the stability of monellin is effectively improved, the purification step is simpler and more convenient, and the method is suitable for industrial production.

The invention belongs to the technical field of biology, and particularly relates to a receptor peptidomimetic capable of improving the breeding efficiency of butter crabs and application of the receptor peptidomimetic. The optimal binding conformation is screened according to the sequence prediction binding conformation of the vitellogen and the receptor of the vitellogen, the hotspot residues are screened according to the optimal binding conformation, and the binding energy change before and after mutation of the hotspot residues is calculated to determine the receptor peptidomimetic sequence. The receptor peptidomimetic can obviously slow down the development speed of the ovary of the blue crab and effectively induce the formation of the butter crab by utilizing the specificity of specific recognition of the vitellogenin of the blue crab and the receptor, so that the butter crab product can be produced in a planned manner.

The present disclosure is directed to HLA class II molecules having a higher affinity for CD4 than naturally occurring HLA class II molecules. In certain aspects, the HLA class II molecule comprises a DQ beta chain having (i) an amino acid other than leucine at a position corresponding to amino acid residue 114 of SEQ ID NO: 1, (ii) an amino acid other than valine at a position corresponding to amino acid residue 143 of SEQ ID NO: 1, (iii) or both (i) and (ii). Certain aspects of the present disclosure are directed to nucleic acid molecules encoding the HLA class II molecules, vectors comprising the nucleic acid molecule, cells comprising the same, and methods of use thereof.

The invention provides an infectious bronchitis virus subunit vaccine as well as a preparation method and application thereof, and belongs to the technical field of genetic engineering vaccines. According to the chicken infectious bronchitis virus mutant protein disclosed by the invention, the amino acid sequence of the mutant protein is shown as SEQ ID NO.5. According to the avian infectious bronchitis virus subunit vaccine containing the recombinant avian infectious bronchitis virus mutant protein Kozak-IgKsp-IBV-M41-S-core-6His as an effective component, the glycosylation level of the vaccine is relatively high, the expression level is relatively stable, the virus return risk of a live vaccine does not exist, the safety is high, large-scale industrial preparation can be achieved, and the vaccine has good application prospects. The cost is low.

The present disclosure is directed to peptide antigens derived from a previously undefined epitope on influenza A virus hemagglutinin and methods for use thereof.

The present invention relates to methods and cross-linkers for the macrocyclization of proteins. The invention is useful for increasing the stability of a protein.

In a method for treating cancer by desialylation of sialylated glycans expressed on the surface of cancer cells, the present invention provides a method for extending the serum half-life of the active ingredient, sialidase, and enhancing the therapeutic effect of said sialidase. [Solution] A pharmaceutical composition is provided that contains sialidase which, when administered to a subject, conjugates to a serum half-life enhancing factor that increases the serum half-life of sialidase.

To provide a CD3 antibody that is capable of binding to primate CD3, has a suitable CD3 binding capacity, and has a stable single-chain scFv structure.SOLUTION: Disclosed are a CD3-targeting antibody, a bispecific antibody and the use thereof. The CD3-targeting antibody comprises a light chain variable region (VL) and a heavy chain variable region (VH). The VL has the amino acid sequence as shown in SEQ ID NO: 56 or a mutation thereof. The VH has mutations on the amino acid sequence as shown in SEQ ID NO: 42, and the mutations occur at one or more of the sites of amino acid residues selected from positions 30, 73, 76, 78, 93 and 94. The bispecific antibody comprises a first protein domain and a second protein domain, wherein the first protein domain comprises the CD3-targeting antibody as described above. The CD3-targeting antibody reduces the toxicity caused by cytokine release syndrome, and the bispecific antibody prepared therefrom is stable and has the ability to bind to T cells, and also reduces the difficulty of producing.SELECTED DRAWING: Figure 11

The present invention provides an hBCMA-binding polypeptide comprising at least one motif that binds to hBCMA, wherein the peptide has the following structure: [N-terminal portion]-[Helix 1]-[Spacer portion]-[Helix 2]-[C-terminal portion], and the hBCMA-binding motif is the portion [Helix 1]-[Spacer portion]-[Helix 2]. The present invention further provides a pharmaceutical composition comprising the hBCMA-binding polypeptide, and the use of the hBCMA-binding polypeptide or the pharmaceutical composition for use as a medicament, particularly for the treatment or prevention of cancer.

The present disclosure relates to compositions and methods for treating viral infections. Compositions and methods for treating viral infections include conjugates comprising a viral neuraminidase inhibitor (e.g., zanamivir, peramivir, or an analog thereof) linked to an Fc monomer, an Fc domain, and an Fc binding peptide, albumin, or an albumin binding peptide. In particular, the conjugates are useful in the treatment of viral infections (e.g., influenza virus infections).

The invention is applicable to the field of genetic engineering, and provides a mycobacterium tuberculosis Mce1A-LS protein nanoparticle, a preparation method and application thereof, the mycobacterium tuberculosis Mce1A-LS protein nanoparticle is formed by sequence fusion of mycobacterium tuberculosis Mce1A protein and LS protein, and the amino acid sequence of the mycobacterium tuberculosis Mce1A-LS protein nanoparticle is shown as SEQ ID NO: 2 in a sequence table. The Mce1A-LS protein nanoparticle provided by the invention is high in immunogenicity, the protein Mce1A with high immunogenicity can induce to generate a synergistic immune effect and is high in safety, and the expressed fusion protein is non-toxic and harmless, so that the biosafety is high, in addition, the immune effect of the Mce1A-LS protein nanoparticle is good, and after the Mce1A-LS protein nanoparticle is used for immunizing a mouse, the immunogenicity of the Mce1A-LS protein nanoparticle is greatly improved. Strong body fluid and / or cellular immune response can be generated, which indicates that after immunization, a specific immune effect can be generated in a mouse body.

Disclosed herein are methods of modulation of the viability of a cell. Further disclosed herein are methods of modulating an immune response. Further disclosed herein are methods of identifying agents capable of modulation of the viability of a cell or an immune response. Further disclosed herein are agents and compositions capable of modulation of the viability of a cell or an immune response.

To provide a system including novel nanopores having different structures and recognition sites that improve sequencing accuracy and / or provide different error profiles.SOLUTION: Provided are systems relating to the field of nanopores and their use in various applications, e.g., analysis of biopolymers and macromolecules, typically by making electrical measurements during translocation through the nanopore, comprising a funnel-shaped proteinaceous nanopore comprising alpha-helical pore-forming toxins that are members from the actinoporin family of proteins, more particularly Fraga Ceatoxin C (FraC), a variant FraC, a FraC paralog or a FraC homolog.SELECTED DRAWING: None

Provided are a single-chain polypeptide which is highly activated after entering a specific use site, attenuated and can be safer and more convenient to produce, and the corresponding use thereof, a nucleic acid encoding same and a preparation method therefor. The single-chain polypeptide comprises: a first domain, an intermediate amino acid sequence region, and a second domain, wherein the intermediate amino acid sequence region is located between the first domain and the second domain, and contains at least one first enzyme cleavage site, the first enzyme cleavage site is designed to be capable of being highly specifically cleaved by a first protease present in a specific part of the human body, and the single-chain polypeptide is converted into an activated form capable of inhibiting the release of an information substance after being cleaved by the first protease at the first enzyme cleavage site.

The invention belongs to the technical field of biology, and particularly relates to a porcine pseudorabies virus gB-gD recombinant fusion protein subunit vaccine as well as a preparation method and application thereof. According to the invention, the PRV gB and gD genes are selected to serially express the gBgD protein to prepare the vaccine, the gB and gD proteins which are respectively expressed are replaced, and the vaccine is high in safety and good in immunogenicity, can effectively prevent the occurrence of a pseudorabies virus virulence enhancement event when being clinically used, provides a powerful space for purification of pseudorabies, and has a wide application prospect.

Provided herein are methods for generating a protein product, comprising: providing a plant seed; contacting said plant seed with a protein expression vector that encodes for a protein; transiently expressing said protein in said plant seed using said protein expression vector, and isolating said protein from said plant seed to obtain a protein product.

The present invention relates to polypeptides for degrading polyesters. Disclosed herein are microbially-derived polypeptides and engineered variants thereof for degrading polyethylene terephthalate (PET) and other polyesters. Also provided are methods of producing the polypeptides and methods for polyester degradation using the polypeptides.

The invention relates to a novel human immunodeficiency virus envelope protein antigen expressed by mammals. Various embodiments of the invention relate to a polypeptide comprising 1-10 epitopes or more of the HIV envelope protein and a fusion protein, wherein the polypeptide lacks a transmembrane domain of the HIV gp41 protein. Such polypeptides can be expressed in mammalian cells, such as human cells, to produce polypeptides useful, for example, in the development of novel anti-HIV antibodies. The polypeptides described herein and the novel antibodies developed therefrom are generally useful in medical diagnostics, and they can also be used in the prophylactic and therapeutic treatment of HIV.

The invention discloses a high-biological-activity human-derived I-type collagen variant, a composite material based on the high-biological-activity human-derived I-type collagen variant and a preparation method. According to the invention, the COL109 fragment which can be efficiently secreted and expressed in pichia pastoris and has a triple helix structure is obtained through screening; an adhesion domain (GPP) 10 is further fused to improve the mechanical strength, and a variant COL109 (GPP) 10 is obtained; and finally, compounding with polycaprolactone (PCL) according to an optimized ratio (1: 1) to obtain the composite material with high biological activity (promoting osteogenic differentiation and wound healing) and excellent mechanical properties. The material is suitable for bone tissue engineering scaffolds, skin regeneration dressings and the like.

Compositions and methods for selective targeting of BMP / TGFβ signaling using heteromeric complexes, preferably heteromeric complexes comprising single-chain variable domain (scFv) antibodies (Abs) that target the extracellular domains of BMP type I and type II receptors.

The application discloses a kind of multi-effect repair type collagen and its application in the technical field of synthetic biology, the application selects transdermal peptide TD-1, the coding gene of the transmembrane region of human XVII type collagen, extracellular sixteenth non-collagen region and extracellular fifteenth collagen region and His tag is connected in series, and gene sequence is optimized by pichia pastoris codon selection preference, then obtains T-COL17R3 by construction and expression. Through efficacy experiment, it is verified that T-COL17R3 compared with similar products on sale, not only excellent transdermal performance, also has more optimal ability of promoting cell proliferation, migration, anti early glycation product ketone amine and anti late glycation product dicarbonyl compound, better free radical scavenging ability and anti-elastase ability, and can reduce the synthesis of melanin in B16-F10 cell, therefore, T-COL17R3 has excellent application potential in the development of drug composition or skin care product with repair, anti-wrinkle firming or whitening effect.

The invention relates to a method for identifying and quantifying a polypeptide from a library of polypeptides. The method comprises the steps of: 1 - providing a polypeptide library and a detection tag library, 2 - generating a nested library comprising the polypeptides and the detection tags, 3 - sequencing the nested library, 4 - selecting a member of the nested library in one or several selection steps that are independent of a physical genotype-phenotype linkage, 5 - isolating the detection tag from the selected polypeptide, 6 - identifying and quantifying the detection tag by mass spectrometry, 7 - obtaining the sequence of the selected polypeptide.

To provide novel PH20 variants or fragments thereof improved in the stability, enzyme activity and expression level compared to mature wild-type PH20.SOLUTION: The invention provides novel PH20 variants or fragments thereof improved in thermal stability and enzymatic activity of human hyaluronidase, which is an enzyme for hydrolyzing hyaluronic acid, the novel PH20 variants or fragments thereof including one or more amino acid residue substitutions in a variant having a specific amino acid sequence, where additional amino acid residues at the N-terminus and / or the C-terminus are optionally deleted.SELECTED DRAWING: Figure 4

The application discloses a sequence of a separated new bunyavirus M segment and a Gn protein coded by the sequence, a nucleotide sequence of the M segment and an amino acid sequence coded by the nucleotide sequence, and expression, purification and activity analysis of a fusion protein formed by fusing the Gn coded by the M segment with Fc to form a Gn-Fc protein. In addition, the application also relates to cross reaction of the fusion protein with polyclonal antibodies in different patient sera.

The invention relates to the field of biological medicine, in particular to an anti-human NaPi2b antibody and application thereof. The invention discloses a humanized monoclonal antibody of an anti-human NaPi2b (Napidab) and a preparation method of the humanized monoclonal antibody of the anti-human NaPi2b. Also disclosed are pharmaceutical compositions comprising the human NaPi2b antibodies, as well as therapeutic and diagnostic methods of using the human NaPi2b antibodies.

Provided herein are methods and compositions relating to enzymes and libraries having nucleic acids encoding the enzymes that include modified sequences. Further provided herein are methods for enzyme optimization. Further provided herein are enzymes for sequencing library generation.